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From Proteopedia
Crystal structure of human odorant binding protein OBPIIa
Structural highlights
FunctionOBP2A_HUMAN Probably binds and transports small hydrophobic volatile molecules with a higher affinity for aldehydes and large fatty acids.[1] Publication Abstract from PubMedHuman odorant-binding protein, OBPIIa , is expressed by nasal epithelia to facilitate transport of hydrophobic odorant molecules across the aqueous mucus. Here, we report its crystallographic analysis at 2.6 A resolution. OBPIIa is a monomeric protein that exhibits the classical lipocalin fold with a conserved eight-stranded beta-barrel harboring a remarkably large hydrophobic pocket. Basic residues within the four loops that shape the entrance to this ligand-binding site evoke a positive electrostatic potential. Human OBPIIa shows distinct features compared with other mammalian OBPs, including a potentially reactive Cys side chain within its pocket similar to human tear lipocalin. Proteins 2015. (c) 2015 Wiley Periodicals, Inc. Crystal structure of the human odorant binding protein, OBP.,Schiefner A, Freier R, Eichinger A, Skerra A Proteins. 2015 Mar 21. doi: 10.1002/prot.24797. PMID:25810031[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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